Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance

Autores
Llerena Suster, Carlos Rafael; Toledo, Victoria; Fittipaldi, Antonela Soledad; Morcelle del Valle, Susana Raquel; Briand, Laura Estefania
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
BACKGROUND The immobilization of the lipase B of Candida antarctica CALB overTiO2 nanoparticles was thoroughly investigated with the isotherms of adsorption at various temperatures with and without the addition of sorbitol and glycerol. The surface composition, secondary structure and the effect of the addition of the polyols was addressed.RESULTS The maximum dispersion limit of protein on TiO2 NPs is 0.073 ± 0.007μmol. Glycerol and sorbitol co-adsorb on the TiO2 NPs reaching 45 % of thesurface composition of the biocatalyst. The optimized material was able to catalyze the esterification of 52 % of R/S-ibuprofen with ethanol (0.31 ± 0.01 μmol.min-1.mg-1) with 41 % of enantiomeric excess towards S(+)-ibuprofen in 24 hs of reaction. Under similar reaction conditions, the commercial counterpart Novozym® 435 showed 34 % of conversion (0.091 ± 0.003 μmol.min-1.mg-1) and 16 % of enantiomeric excess.CONCLUSIONS The molecular association between the protein and the polyolsexerts a positive cooperativism since prevents the aggregation of the protein and protects its active conformation. The residual esterase activity of the immobilized CALB compared with the free lipase depends directly on the amount of co-adsorbed polyols. Moreover, polyols boost the catalytic performance in the kinetic resolution of racemic ibuprofen showing an optimum at the maximum coverage of polyols on the biocatalysts.
Fil: Llerena Suster, Carlos Rafael. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina
Fil: Toledo, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas ; Argentina
Fil: Fittipaldi, Antonela Soledad. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Morcelle del Valle, Susana Raquel. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Briand, Laura Estefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas ; Argentina
Materia
Lipases
Tio2 Nps
Biocatalysis
Immobilization
Adsorption
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/36769
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/36769
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic PerformanceLlerena Suster, Carlos RafaelToledo, VictoriaFittipaldi, Antonela SoledadMorcelle del Valle, Susana RaquelBriand, Laura EstefaniaLipasesTio2 NpsBiocatalysisImmobilizationAdsorptionhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2BACKGROUND The immobilization of the lipase B of Candida antarctica CALB overTiO2 nanoparticles was thoroughly investigated with the isotherms of adsorption at various temperatures with and without the addition of sorbitol and glycerol. The surface composition, secondary structure and the effect of the addition of the polyols was addressed.RESULTS The maximum dispersion limit of protein on TiO2 NPs is 0.073 ± 0.007μmol. Glycerol and sorbitol co-adsorb on the TiO2 NPs reaching 45 % of thesurface composition of the biocatalyst. The optimized material was able to catalyze the esterification of 52 % of R/S-ibuprofen with ethanol (0.31 ± 0.01 μmol.min-1.mg-1) with 41 % of enantiomeric excess towards S(+)-ibuprofen in 24 hs of reaction. Under similar reaction conditions, the commercial counterpart Novozym® 435 showed 34 % of conversion (0.091 ± 0.003 μmol.min-1.mg-1) and 16 % of enantiomeric excess.CONCLUSIONS The molecular association between the protein and the polyolsexerts a positive cooperativism since prevents the aggregation of the protein and protects its active conformation. The residual esterase activity of the immobilized CALB compared with the free lipase depends directly on the amount of co-adsorbed polyols. Moreover, polyols boost the catalytic performance in the kinetic resolution of racemic ibuprofen showing an optimum at the maximum coverage of polyols on the biocatalysts.Fil: Llerena Suster, Carlos Rafael. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; ArgentinaFil: Toledo, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas ; ArgentinaFil: Fittipaldi, Antonela Soledad. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Morcelle del Valle, Susana Raquel. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Briand, Laura Estefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas ; ArgentinaWiley2017-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/36769Llerena Suster, Carlos Rafael; Toledo, Victoria; Fittipaldi, Antonela Soledad; Morcelle del Valle, Susana Raquel; Briand, Laura Estefania; Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance; Wiley; Journal of Chemical Technology and Biotechnology; 29; 11; 6-2017; 2870-28800268-2575CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/jctb.5305info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jctb.5305/abstractinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:06:47Zoai:ri.conicet.gov.ar:11336/36769instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:06:48.278CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
title Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
spellingShingle Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
Llerena Suster, Carlos Rafael
Lipases
Tio2 Nps
Biocatalysis
Immobilization
Adsorption
title_short Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
title_full Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
title_fullStr Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
title_full_unstemmed Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
title_sort Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance
dc.creator.none.fl_str_mv Llerena Suster, Carlos Rafael
Toledo, Victoria
Fittipaldi, Antonela Soledad
Morcelle del Valle, Susana Raquel
Briand, Laura Estefania
author Llerena Suster, Carlos Rafael
author_facet Llerena Suster, Carlos Rafael
Toledo, Victoria
Fittipaldi, Antonela Soledad
Morcelle del Valle, Susana Raquel
Briand, Laura Estefania
author_role author
author2 Toledo, Victoria
Fittipaldi, Antonela Soledad
Morcelle del Valle, Susana Raquel
Briand, Laura Estefania
author2_role author
author
author
author
dc.subject.none.fl_str_mv Lipases
Tio2 Nps
Biocatalysis
Immobilization
Adsorption
topic Lipases
Tio2 Nps
Biocatalysis
Immobilization
Adsorption
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv BACKGROUND The immobilization of the lipase B of Candida antarctica CALB overTiO2 nanoparticles was thoroughly investigated with the isotherms of adsorption at various temperatures with and without the addition of sorbitol and glycerol. The surface composition, secondary structure and the effect of the addition of the polyols was addressed.RESULTS The maximum dispersion limit of protein on TiO2 NPs is 0.073 ± 0.007μmol. Glycerol and sorbitol co-adsorb on the TiO2 NPs reaching 45 % of thesurface composition of the biocatalyst. The optimized material was able to catalyze the esterification of 52 % of R/S-ibuprofen with ethanol (0.31 ± 0.01 μmol.min-1.mg-1) with 41 % of enantiomeric excess towards S(+)-ibuprofen in 24 hs of reaction. Under similar reaction conditions, the commercial counterpart Novozym® 435 showed 34 % of conversion (0.091 ± 0.003 μmol.min-1.mg-1) and 16 % of enantiomeric excess.CONCLUSIONS The molecular association between the protein and the polyolsexerts a positive cooperativism since prevents the aggregation of the protein and protects its active conformation. The residual esterase activity of the immobilized CALB compared with the free lipase depends directly on the amount of co-adsorbed polyols. Moreover, polyols boost the catalytic performance in the kinetic resolution of racemic ibuprofen showing an optimum at the maximum coverage of polyols on the biocatalysts.
Fil: Llerena Suster, Carlos Rafael. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina
Fil: Toledo, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas ; Argentina
Fil: Fittipaldi, Antonela Soledad. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Morcelle del Valle, Susana Raquel. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Briand, Laura Estefania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas ; Argentina
description BACKGROUND The immobilization of the lipase B of Candida antarctica CALB overTiO2 nanoparticles was thoroughly investigated with the isotherms of adsorption at various temperatures with and without the addition of sorbitol and glycerol. The surface composition, secondary structure and the effect of the addition of the polyols was addressed.RESULTS The maximum dispersion limit of protein on TiO2 NPs is 0.073 ± 0.007μmol. Glycerol and sorbitol co-adsorb on the TiO2 NPs reaching 45 % of thesurface composition of the biocatalyst. The optimized material was able to catalyze the esterification of 52 % of R/S-ibuprofen with ethanol (0.31 ± 0.01 μmol.min-1.mg-1) with 41 % of enantiomeric excess towards S(+)-ibuprofen in 24 hs of reaction. Under similar reaction conditions, the commercial counterpart Novozym® 435 showed 34 % of conversion (0.091 ± 0.003 μmol.min-1.mg-1) and 16 % of enantiomeric excess.CONCLUSIONS The molecular association between the protein and the polyolsexerts a positive cooperativism since prevents the aggregation of the protein and protects its active conformation. The residual esterase activity of the immobilized CALB compared with the free lipase depends directly on the amount of co-adsorbed polyols. Moreover, polyols boost the catalytic performance in the kinetic resolution of racemic ibuprofen showing an optimum at the maximum coverage of polyols on the biocatalysts.
publishDate 2017
dc.date.none.fl_str_mv 2017-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/36769
Llerena Suster, Carlos Rafael; Toledo, Victoria; Fittipaldi, Antonela Soledad; Morcelle del Valle, Susana Raquel; Briand, Laura Estefania; Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance; Wiley; Journal of Chemical Technology and Biotechnology; 29; 11; 6-2017; 2870-2880
0268-2575
CONICET Digital
CONICET
url http://hdl.handle.net/11336/36769
identifier_str_mv Llerena Suster, Carlos Rafael; Toledo, Victoria; Fittipaldi, Antonela Soledad; Morcelle del Valle, Susana Raquel; Briand, Laura Estefania; Lipase B of Candida antarctica Co-adsorbed with Polyols onto TiO2 Nanoparticles for Improved Biocatalytic Performance; Wiley; Journal of Chemical Technology and Biotechnology; 29; 11; 6-2017; 2870-2880
0268-2575
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/jctb.5305
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jctb.5305/abstract
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.993085

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